Detail of "15839-70-0"

Reference

Inhibition of L-fucose incorporation into glycoprotein of sarcoma 180 ascites cells by 6-thioguanine

Inhibition of L-fucose incorporation into glycoprotein of sarcoma 180 ascites cells by 6-thioguanine. Lazo, John Stephen; Hwang, Kou M.; Sartorelli, Alan C. (Comp. Cancer Cent., Yale Univ. Sch. Med., New Haven, Conn., USA). Cancer Res., 37(12), 4250-5 (English) 1977. CODEN: CNREA8. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacodynamics) To gain evidence for the role of membrane lesions in the cytotoxic action of 6-thioguanine (I) [154-42-7], the effects of I on fucose [2438-80-4] metab. were examd. in a transplanted neoplasm. Exposure of sarcoma 180 cells to I in mice inhibited fucose, but not glucosamine, incorporation into cell glycoproteins. Such an inhibition of the incorporation of a terminal carbohydrate may be involved in the modification of surface structure by I. The inhibition by I of fucose utilization for glycoprotein formation appears to be largely due to a decrease in the formation of GDP-fucose [15839-70-0].

Effect of atractylosides, palmitoyl coenzyme A, and anion transport inhibitors on translocation of nucleotide sugars and nucleotide sulfate into Golgi vesicles

Effect of atractylosides, palmitoyl coenzyme A, and anion transport inhibitors on translocation of nucleotide sugars and nucleotide sulfate into Golgi vesicles. Capasso, Juan M.; Hirschberg, Carlos B. (Sch. Med., Saint Louis Univ., St. Louis, MO 63104, USA). 15839-70-0 and 482-67-7 are cas registry numbers. These chemicals are also mentioned in this article. J. Biol. Chem., 259(7), 4263-6 (English) 1984. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) The effect of palmitoyl coA, atractylosides, and anion transport inhibitors on translocation into rat liver Golgi vesicles of adenosine 3'-phosphate 5'-phosphosulfate (PAPS), CMP-N-acetylneuraminic acid, and GDP-fucose was studied. Translocation of the above 3 nucleotide derivs. was inhibited by DIDS; 50% inhibition required 10-20 mM DIDS. The inhibition of translocation of PAPS by DIDS was used to demonstrate that sulfation of macromols. within Golgi vesicles is preceded by translocation of PAPS into the vesicles. Palmitoyl coA, at concns. below its crit. micellar concns., specifically inhibited translocation into Golgi vesicles of PAPS but not CMP-NeuAc and GDP-fucose. Inhibition of PAPS translocation by 50% required 9 mM palmitoyl CoA. Translocation of PAPS but not of CMP-NeuAc or GDP-fucose was also inhibited by atractyloside or carboxyatractyloside with 50% inhibition requiring 15 mM of either glycoside. This pattern of inhibition suggests structural similarities between the putative translocator of PAPS in Golgi membranes and the ATP/ADP translocator of mitochondria. .